Mammalian Rad51 protein: a RecA homologue with pleiotropic functions.
During the last years, homologues of E coli RecA have been cloned in numerous species including man. These Rad51 proteins share sequence as well as functional homologies with the bacterial protein. Human Rad51 (HsRad51) is able to catalyze strand exchange in vitro between homologous DNAs, but with a lower efficiency compared to that of RecA. This suggests the requirement of additional factors. A very interesting feature of Rad51 is its essential role in mouse which could mean that it has gained an essential function in cell growth. The interaction of HsRad51 with several tumor suppressor genes namely p53, BRCA1 and BRCA2 implies possible role(s) of this protein in tumorigenesis. Thus, the continued study of Rad51 should bring important insights not only into homologous recombination mechanisms but also into cell proliferation regulation.
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Institut de Pharmacologie et de Biologie Structurale, CNRS, UPR 9062, Toulouse, France.
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D000818:Animals; D004254:DNA Nucleotidyltransferases / Q000235:genetics / Q000502:physiology; D004268:DNA-Binding Proteins / Q000235:genetics* / Q000502:physiology*; D005656:Fungal Proteins / Q000235:genetics* / Q000502:physiology*; D006801:Humans; D051135:Rad51 Recombinase; D011938:Rec A Recombinases / Q000235:genetics*; D012441:Saccharomyces cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D017386:Sequence Homology, Amino Acid
D004268:DNA-Binding Proteins; D005656:Fungal Proteins; D029701:Saccharomyces cerevisiae Proteins; D004254:DNA Nucleotidyltransferases; C495151:RAD51 protein, S cerevisiae; C495153:RAD51 protein, human; D051135:Rad51 Recombinase; D011938:Rec A Recombinases